SL9B2_MOUSE
ID SL9B2_MOUSE Reviewed; 547 AA.
AC Q5BKR2; Q8CA47; Q8CDX4;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Sodium/hydrogen exchanger 9B2;
DE AltName: Full=NHA-oc {ECO:0000303|PubMed:17988971};
DE AltName: Full=Na(+)/H(+) exchanger NHA2;
DE AltName: Full=Na(+)/H(+) exchanger-like domain-containing protein 2;
DE Short=NHE domain-containing protein 2;
DE AltName: Full=Soditlum/hydrogen exchanger-like domain-containing protein 2;
DE AltName: Full=Solute carrier family 9 subfamily B member 2;
GN Name=Slc9b2 {ECO:0000312|MGI:MGI:2140077}; Synonyms=Nha2, Nhedc2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Head, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Molar;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=17698421; DOI=10.1016/j.modgep.2007.07.002;
RA Pham L., Purcell P., Morse L., Stashenko P., Battaglino R.A.;
RT "Expression analysis of nha-oc/NHA2: a novel gene selectively expressed in
RT osteoclasts.";
RL Gene Expr. Patterns 7:846-851(2007).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=18000046; DOI=10.1073/pnas.0707120104;
RA Xiang M., Feng M., Muend S., Rao R.;
RT "A human Na+/H+ antiporter sharing evolutionary origins with bacterial NhaA
RT may be a candidate gene for essential hypertension.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18677-18681(2007).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=17988971; DOI=10.1016/j.bone.2007.09.046;
RA Battaglino R.A., Pham L., Morse L.R., Vokes M., Sharma A., Odgren P.R.,
RA Yang M., Sasaki H., Stashenko P.;
RT "NHA-oc/NHA2: a mitochondrial cation-proton antiporter selectively
RT expressed in osteoclasts.";
RL Bone 42:180-192(2008).
RN [7]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION, AND INDUCTION.
RX PubMed=18508966; DOI=10.1681/asn.2007111245;
RA Fuster D.G., Zhang J., Shi M., Bobulescu I.A., Andersson S., Moe O.W.;
RT "Characterization of the sodium/hydrogen exchanger NHA2.";
RL J. Am. Soc. Nephrol. 19:1547-1556(2008).
RN [8]
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INDUCTION, AND FUNCTION.
RX PubMed=20441802; DOI=10.1016/j.bone.2010.04.605;
RA Hofstetter W., Siegrist M., Simonin A., Bonny O., Fuster D.G.;
RT "Sodium/hydrogen exchanger NHA2 in osteoclasts: subcellular localization
RT and role in vitro and in vivo.";
RL Bone 47:331-340(2010).
RN [9]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=22985540; DOI=10.1016/j.bone.2012.08.113;
RA Charles J.F., Coury F., Sulyanto R., Sitara D., Wu J., Brady N., Tsang K.,
RA Sigrist K., Tollefsen D.M., He L., Storm D., Aliprantis A.O.;
RT "The collection of NFATc1-dependent transcripts in the osteoclast includes
RT numerous genes non-essential to physiologic bone resorption.";
RL Bone 51:902-912(2012).
RN [10]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23720317; DOI=10.1073/pnas.1220009110;
RA Deisl C., Simonin A., Anderegg M., Albano G., Kovacs G., Ackermann D.,
RA Moch H., Dolci W., Thorens B., Hediger M.A., Fuster D.G.;
RT "Sodium/hydrogen exchanger NHA2 is critical for insulin secretion in beta-
RT cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:10004-10009(2013).
RN [11]
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=27010853; DOI=10.1038/cddis.2016.65;
RA Chen S.R., Chen M., Deng S.L., Hao X.X., Wang X.X., Liu Y.X.;
RT "Sodium-hydrogen exchanger NHA1 and NHA2 control sperm motility and male
RT fertility.";
RL Cell Death Dis. 7:E2152-E2152(2016).
CC -!- FUNCTION: Na(+)/H(+) antiporter that extrudes Na(+) or Li(+) in
CC exchange for external protons across the membrane (PubMed:18508966,
CC PubMed:17988971). Contributes to the regulation of intracellular pH,
CC sodium homeostasis, and cell volume. Plays an important role for
CC insulin secretion and clathrin-mediated endocytosis in beta-cells
CC (PubMed:23720317). Involved in sperm motility and fertility
CC (PubMed:27010853). It is controversial whether SLC9B2 plays a role in
CC osteoclast differentiation (PubMed:17988971) or not (PubMed:20441802,
CC PubMed:22985540). {ECO:0000269|PubMed:17988971,
CC ECO:0000269|PubMed:18508966, ECO:0000269|PubMed:20441802,
CC ECO:0000269|PubMed:22985540, ECO:0000269|PubMed:23720317,
CC ECO:0000269|PubMed:27010853}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q86UD5}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18508966,
CC ECO:0000269|PubMed:20441802}; Multi-pass membrane protein
CC {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:17988971};
CC Multi-pass membrane protein {ECO:0000255}. Endosome membrane
CC {ECO:0000269|PubMed:23720317}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC membrane {ECO:0000269|PubMed:23720317}; Multi-pass membrane protein.
CC Cell projection, cilium, flagellum membrane
CC {ECO:0000269|PubMed:27010853}; Multi-pass membrane protein
CC {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:20441802};
CC Multi-pass membrane protein {ECO:0000255}. Note=Strong colocalization
CC with LAMP1 and TCIRG1 in osteoclasts (PubMed:20441802). In beta-cells
CC colocalizes with RAB4A and SYP (PubMed:23720317). Localizes to the
CC basolateral membrane of polarized osteoclasts (PubMed:20441802). On the
CC contrary to (PubMed:17988971) not detected at the mitochondrion
CC membrane (PubMed:20441802, PubMed:23720317).
CC {ECO:0000269|PubMed:17988971, ECO:0000269|PubMed:20441802,
CC ECO:0000269|PubMed:23720317}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5BKR2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5BKR2-2; Sequence=VSP_033155;
CC Name=3;
CC IsoId=Q5BKR2-3; Sequence=VSP_033154;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:18000046, PubMed:18508966,
CC PubMed:17988971). However expression seems to be restricted to specific
CC cell types within individual organs, e.g. osteoclasts in the bone,
CC distal tubules of the kidney or beta-cells of Langerhans islets
CC (PubMed:18508966, PubMed:17988971, PubMed:17698421, PubMed:23720317).
CC In sperm specifically present in the principal piece of sperm tail (at
CC protein level) (PubMed:27010853). {ECO:0000269|PubMed:17698421,
CC ECO:0000269|PubMed:17988971, ECO:0000269|PubMed:18000046,
CC ECO:0000269|PubMed:18508966, ECO:0000269|PubMed:23720317,
CC ECO:0000269|PubMed:27010853}.
CC -!- INDUCTION: Not detectable during the early stages of osteoclast
CC differentiation induced by TNFSF11/RANKL (PubMed:17698421,
CC PubMed:17988971). Up-regulated during the later stages of osteoclast
CC differentiation (PubMed:20441802, PubMed:18508966, PubMed:17698421,
CC PubMed:17988971). Up-regulated in macrophages and blood mononuclear
CC cells treated with TNFSF11/RANKL. {ECO:0000269|PubMed:17698421,
CC ECO:0000269|PubMed:17988971, ECO:0000269|PubMed:18508966,
CC ECO:0000269|PubMed:20441802}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. However males show reduced
CC fertility caused by diminished sperm motility (PubMed:27010853).
CC Deficient mice display a pathological glucose tolerance with impaired
CC insulin secretion but normal peripheral insulin sensitivity
CC (PubMed:23720317). Mutant have normal bone density and their bones are
CC characterized by normal structural parameters (PubMed:20441802,
CC PubMed:22985540). {ECO:0000269|PubMed:20441802,
CC ECO:0000269|PubMed:22985540, ECO:0000269|PubMed:23720317,
CC ECO:0000269|PubMed:27010853}.
CC -!- MISCELLANEOUS: Inhibited by phloretin but not by the classical SLC9A-
CC inhibitor amiloride. {ECO:0000250|UniProtKB:Q86UD5}.
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1)
CC transporter (TC 2.A.36) family. {ECO:0000305}.
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DR EMBL; AK029417; BAC26441.1; -; mRNA.
DR EMBL; AK039655; BAC30408.1; -; mRNA.
DR EMBL; AC104874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC090977; AAH90977.1; -; mRNA.
DR CCDS; CCDS17854.1; -. [Q5BKR2-1]
DR RefSeq; NP_849208.4; NM_178877.6. [Q5BKR2-1]
DR RefSeq; XP_006502461.1; XM_006502398.3. [Q5BKR2-1]
DR RefSeq; XP_006502462.1; XM_006502399.3. [Q5BKR2-1]
DR AlphaFoldDB; Q5BKR2; -.
DR SMR; Q5BKR2; -.
DR STRING; 10090.ENSMUSP00000060640; -.
DR PhosphoSitePlus; Q5BKR2; -.
DR EPD; Q5BKR2; -.
DR PaxDb; Q5BKR2; -.
DR PeptideAtlas; Q5BKR2; -.
DR PRIDE; Q5BKR2; -.
DR ProteomicsDB; 261067; -. [Q5BKR2-1]
DR ProteomicsDB; 261068; -. [Q5BKR2-2]
DR ProteomicsDB; 261069; -. [Q5BKR2-3]
DR Antibodypedia; 26081; 162 antibodies from 24 providers.
DR DNASU; 97086; -.
DR Ensembl; ENSMUST00000051849; ENSMUSP00000060640; ENSMUSG00000037994. [Q5BKR2-1]
DR GeneID; 97086; -.
DR KEGG; mmu:97086; -.
DR UCSC; uc008rld.2; mouse. [Q5BKR2-1]
DR UCSC; uc008rle.2; mouse. [Q5BKR2-3]
DR CTD; 133308; -.
DR MGI; MGI:2140077; Slc9b2.
DR VEuPathDB; HostDB:ENSMUSG00000037994; -.
DR eggNOG; KOG3826; Eukaryota.
DR GeneTree; ENSGT00390000013285; -.
DR HOGENOM; CLU_018415_4_1_1; -.
DR InParanoid; Q5BKR2; -.
DR OMA; GWTIDDN; -.
DR OrthoDB; 833306at2759; -.
DR PhylomeDB; Q5BKR2; -.
DR TreeFam; TF319087; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR BioGRID-ORCS; 97086; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Slc9b2; mouse.
DR PRO; PR:Q5BKR2; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q5BKR2; protein.
DR Bgee; ENSMUSG00000037994; Expressed in hindlimb long bone and 97 other tissues.
DR ExpressionAtlas; Q5BKR2; baseline and differential.
DR Genevisible; Q5BKR2; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0097708; C:intracellular vesicle; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0097228; C:sperm principal piece; IMP:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0010348; F:lithium:proton antiporter activity; ISS:UniProtKB.
DR GO; GO:0015385; F:sodium:proton antiporter activity; ISS:UniProtKB.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IDA:UniProtKB.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:UniProtKB.
DR GO; GO:2001206; P:positive regulation of osteoclast development; IDA:MGI.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IDA:UniProtKB.
DR GO; GO:0006814; P:sodium ion transport; ISO:MGI.
DR Gene3D; 1.20.1530.20; -; 1.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR038770; Na+/solute_symporter_sf.
DR InterPro; IPR037072; SLC9B2.
DR PANTHER; PTHR31102:SF14; PTHR31102:SF14; 1.
DR Pfam; PF00999; Na_H_Exchanger; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiport; Cell membrane; Cell projection; Cilium;
KW Cytoplasmic vesicle; Endosome; Flagellum; Hydrogen ion transport;
KW Ion transport; Membrane; Mitochondrion; Phosphoprotein; Reference proteome;
KW Sodium; Sodium transport; Synapse; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..547
FT /note="Sodium/hydrogen exchanger 9B2"
FT /id="PRO_0000331271"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 278
FT /note="Important for cation transport"
FT /evidence="ECO:0000250|UniProtKB:Q86UD5"
FT SITE 279
FT /note="Important for cation transport"
FT /evidence="ECO:0000250|UniProtKB:Q86UD5"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UD5"
FT VAR_SEQ 1..438
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033154"
FT VAR_SEQ 1..252
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033155"
FT CONFLICT 30
FT /note="Q -> R (in Ref. 3; AAH90977)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 547 AA; 58934 MW; B1F2A99BBF70BE96 CRC64;
MEDEDKTAEC QHSKPPTGIT HEAPPHHELQ EERVMSLRGT DRSEPTEGSN LLTSGEKKPQ
DSPTEPNGLQ SLRRFLACPP RGCLARVITN GTMVVLLWAM VWSVTGPECL PGGNLFGIII
LFYCSITGGK LFGLIKFPTL PPLPPLLGML LAGFLLRNIP VINDSVRIQH KWSSSLRSIA
LSVILVRAGL GLDSKALRKL KGVCVRLAMG PCIVEACASA ILSHFLMGLP WQWGFILGFV
VGAVSPAVVV PSMLLLQEGG YGVGKGIPTL LMAAGSFDDI LAITGFNTCL GVAFSTGSTV
FNIFRGILEV VIGVAAGSFL GFFIQYFPSR DQDNLVWKRA FLVLGFAVLA VFSSVYFSFP
GSGGLCTLVM AFLAGMRWTD KKSEVEKVIA VTWDVFQPLL FGLIGAEVSI VSLRAETVGL
CVATLSIAVL IRILTTFLMV CFAGFNIKEK IFISFAWLPK ATVQAAIGSV ALDTARSHGE
KQLEDYGMDV LTVAFLAILI TAPIGSLLIG LLGPRVLQKS EHRTEEEVQG ETSAHIQRKP
EDSITEA
